Alcohol dehydrogenases from Kluyveromyces marxianus: heterologous expression in Escherichia coliand biochemical characterization

Table 1 Summary of enzymatic properties of KmAdhs and ADHs from other yeasts

ADHs	Optimum temperature (°C)	Optimum pH	Ethanol			Acetaldehyde
			K_m(mM)	K_cat(min^-1)	K_cat/K_m(min^-1 mM^-1)	K_m(mM)	K_cat(min^-1)	K_cat/K_m(min^-1 mM^-1)
KmAdh1^a	50	8.0	39.7	8.5 × 10³	2.1 × 10²	4.0	1.7 × 10⁴	4.3 × 10³
KmAdh2^a	45	7.0	49.5	2.7 × 10²	5.4	1.2	3.2 × 10³	2.7 × 10³
KmAdh3^a	55	7.0	26.0	2.0 × 10³	0.8 × 10²	n.a.
KmAdh4^a	45	7.0	17.0	9.5 × 10³	5.6 × 10²	n.a.
KlAdhI^b	n.d.	n.d.	27	2.5 × 10⁵	9.3 × 10³	1.2	3.6 × 10⁵	3.0 × 10⁵
KlAdhII^b	n.d.	n.d.	23	2.8 × 10⁴	1.2 × 10³	1.7	3.3 × 10⁴	2.0 × 10⁴
KlAdhIII^b,c	n.d.	n.d.	0.5-2.6	8.2 × 10⁴	3.2 × 10⁴	0.1-2.3	8.6 × 10⁵	8.6 × 10⁶
KlAdhIV^b	n.d.	n.d.	1.6	1.3 × 10⁴	8.3 × 10³	3.1	2.9 × 10⁴	9.0 × 10³
SceAdh1^d	30	7.3	17-24	2.0 × 10⁴	1.2 × 10³	1.1-3.4	1.0 × 10⁵	9.3 × 10⁴
SceAdh2^d	30	7.3	0.8	7.8 × 10³	9.6 × 10³	0.1	6.2 × 10⁴	6.9 × 10⁵
SceAdh3^d	30	7.3	12	n.d.	n.d.	0.4	n.d.	n.d.
SpAdh^d	30	7.3	14	n.d.	n.d.	1.6	n.d.	n.d.
HpAdh1^e	n.d.	n.d.	0.3	2.1 × 10⁵	8.4 × 10⁵	1.9	2.0 × 10⁵	1.0 × 10⁵
ScbAdh1^f	n.d.	n.d.	18	2.9 × 10⁴	1.6 × 10³	1.1	2.1 × 10⁵	1.9 × 10⁵

^aData in this study; ^bData from Bozzi et al.[26]; ^cData from Brisdelli et al.[27]; ^dData from Ganzhorn et al.[28] and Thomson JM et al.[22]; ^eData from Suwannarangsee et al.[21]; ^fData from Pal et al.[29]. Kinetic parameters of KmADH1 for ethanol and acetaldehyde were determined in the presence of 2 mM NAD⁺ or 0.2 mM NADH. KmAdh, ADH of K. marxianus; KlAdh, ADH of K. lactis; SceAdh, ADH of S. cerevisiae; SpAdh, ADH of S. pombe; HpAdh, ADH of H. polymorpha; ScbAdh, ADH of S. carlsbergensis; n.a., no activity detected; n.d., no data available.

ISSN: 1472-6750